title: Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation.
abstract: Selective protein cleavage at methionine residues is a useful method for the production of bacterially derived protein fragments containing an N-terminal cysteine residue required for native chemical ligation. Here we describe an optimised procedure for cyanogen bromide-mediated protein cleavage, and ligation of the resulting fragments to afford biologically active proteins.
authors.affiliation: Department of Chemistry, University College London, 20 Gordon Street, London, UK WC1H 0AJ.
authors.forename: Jonathan P
authors.initials: JP
authors.lastname: Richardson
authors.forename: Derek
authors.initials: D
authors.lastname: Macmillan
mesh_terms: D000480:Alkynes / Q000737:chemistry; D003488:Cyanogen Bromide / Q000737:chemistry; D004921:Erythropoietin / Q000138:chemical synthesis* / Q000378:metabolism; D004952:Esters / Q000737:chemistry; D005231:Fatty Acids, Unsaturated / Q000737:chemistry; D020673:Protein Renaturation
chemical_list: D000480:Alkynes; D004952:Esters; D005231:Fatty Acids, Unsaturated; D004921:Erythropoietin; C031203:2-hexadecynoic acid; D003488:Cyanogen Bromide